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PMID:11118213
| Citation |
Kanai, F, Marignani, PA, Sarbassova, D, Yagi, R, Hall, RA, Donowitz, M, Hisaminato, A, Fujiwara, T, Ito, Y, Cantley, LC and Yaffe, MB (2000) TAZ: a novel transcriptional co-activator regulated by interactions with 14-3-3 and PDZ domain proteins. EMBO J. 19:6778-91 |
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| Abstract |
The highly conserved and ubiquitously expressed 14-3-3 proteins regulate differentiation, cell cycle progression and apoptosis by binding intracellular phosphoproteins involved in signal transduction. By screening in vitro translated cDNA pools for the ability to bind 14-3-3, we identified a novel transcriptional co-activator, TAZ (transcriptional co-activator with PDZ-binding motif) as a 14-3-3-binding molecule. TAZ shares homology with Yes-associated protein (YAP), contains a WW domain and functions as a transcriptional co-activator by binding to the PPXY motif present on transcription factors. 14-3-3 binding requires TAZ phosphorylation on a single serine residue, resulting in the inhibition of TAZ transcriptional co-activation through 14-3-3-mediated nuclear export. The C-terminus of TAZ contains a highly conserved PDZ-binding motif that localizes TAZ into discrete nuclear foci and is essential for TAZ-stimulated gene transcription. TAZ uses this same motif to bind the PDZ domain-containing protein NHERF-2, a molecule that tethers plasma membrane ion channels and receptors to cytoskeletal actin. TAZ may link events at the plasma membrane and cytoskeleton to nuclear transcription in a manner that can be regulated by 14-3-3. |
| Links |
PubMed PMC305881 Online version:10.1093/emboj/19.24.6778 |
| Keywords |
14-3-3 Proteins; Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Cell Line; Chickens; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; Gene Expression Regulation; HeLa Cells; Humans; Mice; Molecular Sequence Data; Phosphorylation; Proteins; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Transcription Factors/chemistry; Transcription Factors/metabolism; Tyrosine 3-Monooxygenase/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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See also
References
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